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1LIK

STRUCTURE OF T. GONDII ADENOSINE KINASE BOUND TO ADENOSINE

Replaces:  1DH0
Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0004001molecular_functionadenosine kinase activity
A0005524molecular_functionATP binding
A0005634cellular_componentnucleus
A0005829cellular_componentcytosol
A0006144biological_processpurine nucleobase metabolic process
A0006166biological_processpurine ribonucleoside salvage
A0016301molecular_functionkinase activity
A0016740molecular_functiontransferase activity
A0034654biological_processnucleobase-containing compound biosynthetic process
A0044209biological_processAMP salvage
A0046872molecular_functionmetal ion binding
A0055086biological_processnucleobase-containing small molecule metabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 999
ChainResidue
AARG136
AASN223
AGLY317
AHOH1034
AHOH1056
AHOH1098

site_idAC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL A 899
ChainResidue
AASP35
ALYS80

site_idAC3
Number of Residues14
DetailsBINDING SITE FOR RESIDUE ADN A 699
ChainResidue
AILE22
AASP24
AGLY68
AGLY69
ASER70
AASN73
ATHR140
ATYR169
AASP318
AHOH1038
AHOH1040
AHOH1041
AHOH1056
AASN20

site_idAC4
Number of Residues8
DetailsBINDING SITE FOR RESIDUE ADN A 799
ChainResidue
AGLY280
AHIS281
AVAL302
AASN342
AALA345
AGLN346
AHOH1032
AHOH1076

Functional Information from PROSITE/UniProt
site_idPS00584
Number of Residues14
DetailsPFKB_KINASES_2 pfkB family of carbohydrate kinases signature 2. DTnGAGDafvGGFL
ChainResidueDetails
AASP312-LEU325

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"evidences":[{"source":"PubMed","id":"10669608","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"10669608","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"10794412","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1DGM","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1LII","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1LIK","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"10669608","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1LII","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1LIK","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"10669608","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1LIK","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"10669608","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1LII","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"10794412","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1DGM","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1lio
ChainResidueDetails
AARG136
AASP318

site_idCSA2
Number of Residues4
DetailsAnnotated By Reference To The Literature 1lio
ChainResidueDetails
AALA316
AGLY317
AGLY315
AASP318

site_idMCSA1
Number of Residues2
DetailsM-CSA 209
ChainResidueDetails
AARG136electrostatic stabiliser, hydrogen bond donor
AASP318hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor

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PDB entries from 2026-02-04

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